5.1.99.1	Co2+	most potent activator, Km: 0.0002 mM, binds 2 mol Co2+ per mol of racemase	2434	
5.1.99.1	Mn2+	increases activity to a smaller extent than Co2+	2437	
5.1.99.1	additional information	enzyme does not require tightly bound metal ions for activity, they are not released even after extensive dialysis at pH 2.4	2437	
5.1.99.1	Ni2+	increases activity to a smaller extent than Co2+	2437	
5.1.99.1	Zn2+	increases activity to a smaller extent than Co2+	2437	
5.1.99.1	Co2+	increases activity	2437, 2442	
5.1.99.1	Co3+	lower level of activation than Co2+ at higher concentrations	2442	
5.1.99.1	Fe2+	lower level of activation than Co2+ at higher concentrations	2442	
5.1.99.1	Mn2+	lower level of activation than Co2+ at higher concentrations	2442	
5.1.99.1	additional information	His12, Gln65, His91 and Glu141 provide a binding site for a divalent metal ion, as shown by binding of Co2+	653930	
5.1.99.1	Co2+	0.4 mM, 4fold increase in activity. Presence of Co2+ restores activity after incubation with EDTA	693174	
5.1.99.1	Mn2+	presence of Mn2+ restores activity after incubation with EDTA	693174	
5.1.99.1	additional information	no activation of enzyme with Mg2+, Ni2+	693174	
5.1.99.1	Co2+	enzyme is metal-dependent enzyme, in the active site, metal binding site binds the coenzyme Co2+	706660	
5.1.99.1	Co2+	activates	726729	
5.1.99.1	Co2+	the enzyme is activated by divalent cations (Ni2+, Co2+, and Mg2+)	726729	
5.1.99.1	Mg2+	activates	726729	
5.1.99.1	Mg2+	the enzyme is activated by divalent cations (Ni2+, Co2+, and Mg2+)	726729	
5.1.99.1	Ni2+	activates	726729	
5.1.99.1	Ni2+	the enzyme is activated by divalent cations (Ni2+, Co2+, and Mg2+)	726729